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Related Concept Videos

Improving Translational Accuracy02:07

Improving Translational Accuracy

Base complementarity between the three base pairs of mRNA codon and the tRNA anticodon is not a failsafe mechanism. Inaccuracies can range from a single mismatch to no correct base pairing at all. The free energy difference between the correct and nearly correct base pairs can be as small as 3 kcal/ mol. With complementarity being the only proofreading step, the estimated error frequency would be one wrong amino acid in every 100 amino acids incorporated. However, error frequencies observed in...
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During most eukaryotic translation processes, the small 40S ribosome subunit scans an mRNA from its 5' end until it encounters the first start AUG codon. The large 60S ribosomal subunit then joins the smaller one to initiate protein synthesis. The location of the translation initiation is largely determined by the nucleotides near the start codon as there may be multiple translation initiation sites present on the mRNA.  Marilyn Kozak discovered that the sequence RCCAUGG (where R stands for...
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The large ribosomal subunit has several important structures essential to translation. These include the peptidyl transferase center (PTC) - which is the site where the peptide bond is formed - and a large, internal, water-filled tube through which the nascent polypeptide moves. This latter structure is called the Peptide Exit Tunnel, and it begins at the PTC and spans the body of the large ribosomal subunit. During translation, as the nascent polypeptide chain is synthesized, it passes through...
Initiation of Translation02:33

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Initiating translation is complex because it involves multiple molecules. Initiator tRNA, ribosomal subunits, and eukaryotic initiation factors (eIFs) are all required to assemble on the initiation codon of mRNA. This process consists of several steps that are mediated by different eIFs.
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Toeprinting Analysis of Translation Initiation Complex Formation on Mammalian mRNAs
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Published on: May 10, 2018

Kinetics of stop codon recognition by release factor 1.

Byron Hetrick1, Kristin Lee, Simpson Joseph

  • 1Department of Chemistry and Biochemistry, University of California, San Diego, 9500 Gilman Drive, La Jolla, California 92093-0314, USA.

Biochemistry
|October 31, 2009
PubMed
Summary

Class I release factors (RFs) efficiently distinguish stop from sense codons during protein synthesis. RF1 binds stop codons more stably than sense codons, preventing premature protein termination.

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Area of Science:

  • Molecular Biology
  • Protein Synthesis
  • Genetics

Background:

  • Protein synthesis termination relies on class I release factors (RFs) recognizing stop codons.
  • Efficient discrimination between stop and sense codons is crucial to prevent costly premature termination.

Purpose of the Study:

  • To elucidate the mechanism by which RF1 discriminates between stop and sense codons.
  • To investigate the kinetics of RF1 interaction with the ribosome during translation termination.

Main Methods:

  • Development of a novel pre-steady state kinetic assay.
  • Monitoring the interaction of RF1 with ribosomes programmed with stop and sense codons.

Main Results:

  • RF1 association rates with ribosomes were similar for stop and sense codons.
  • Dissociation rates of RF1 from sense codons were significantly faster (up to 1000-fold) than from stop codons.
  • Sense codon affinity did not correlate with impaired peptide release, indicating a dual discrimination mechanism.

Conclusions:

  • Sense codons inhibit stable RF1 binding and peptide release catalysis.
  • Discrimination involves faster dissociation and reduced peptide release rates.
  • This mechanism ensures accurate protein synthesis termination.